Annotations: 6E0T

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth X]	SCOP2 Family	Ofd1 C-terminal domain-like	8099147	4004393	SCOP2 (2022-06-29)
A [auth X]	SCOP2 Superfamily	Clavaminate synthase-like	8099148	3001848	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth X]	PF10637	e6e0tX1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: PF10637	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth X]	PF10637	Oxoglutarate and iron-dependent oxygenase degradation C-term (Ofd1_CTDD)	Oxoglutarate and iron-dependent oxygenase degradation C-term	Ofd1 is a prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygenase that accelerates the degradation of Sre1N in the presence of oxygen. The domain is conserved from yeasts to humans. Yeast Sre1 is the orthologue of mammalian sterol regulatory ele ...	Ofd1 is a prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygenase that accelerates the degradation of Sre1N in the presence of oxygen. The domain is conserved from yeasts to humans. Yeast Sre1 is the orthologue of mammalian sterol regulatory element binding protein (SREBP), and it responds to changes in oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. However, unlike the prolyl 4-hydroxylases that regulate mammalian hypoxia-inducible factor, Ofd1 uses multiple domains to regulate Sre1N degradation by oxygen; the Ofd1 N-terminal dioxygenase domain is required for oxygen sensing and this Ofd1 C-terminal domain accelerates Sre1N degradation in yeasts [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth X]	Prolyl 3,4-dihydroxylase ofd1	small molecule sensor activity oxygen sensor activity cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity catalytic activity, acting on a protein oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen peptidyl-proline dioxygenase activity catalytic activity small molecule sensor activity oxygen sensor activity cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity catalytic activity, acting on a protein oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen peptidyl-proline dioxygenase activity catalytic activity 2-oxoglutarate-dependent dioxygenase activity dioxygenase activity organic acid binding carbohydrate binding vitamin binding organic cyclic compound binding anion binding monosaccharide binding carboxylic acid binding heterocyclic compound binding L-ascorbic acid binding molecular sequestering activity protein sequestering activity	peptidyl-proline di-hydroxylation organonitrogen compound metabolic process primary metabolic process organic substance metabolic process macromolecule modification peptidyl-proline hydroxylation peptidyl-amino acid modification protein hydroxylation peptidyl-proline modification metabolic process protein metabolic process macromolecule metabolic process protein modification process cellular response to stimulus peptidyl-proline di-hydroxylation organonitrogen compound metabolic process primary metabolic process organic substance metabolic process macromolecule modification peptidyl-proline hydroxylation peptidyl-amino acid modification protein hydroxylation peptidyl-proline modification metabolic process protein metabolic process macromolecule metabolic process protein modification process cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of biological process regulation of cellular response to stress regulation of signal transduction negative regulation of cell communication cell communication negative regulation of SREBP signaling pathway cellular response to stress response to stress regulation of response to stress ER-nucleus signaling pathway negative regulation of cellular process signal transduction regulation of biological process regulation of signaling cellular response to sterol depletion negative regulation of response to stimulus biological regulation negative regulation of signal transduction response to sterol depletion regulation of SREBP signaling pathway SREBP signaling pathway regulation of response to stimulus regulation of cell communication cellular process response to decreased oxygen levels cellular response to oxygen levels cellular response to hypoxia cellular response to decreased oxygen levels cellular response to chemical stimulus response to hypoxia response to chemical response to oxygen levels response to abiotic stimulus regulation of cellular component organization cellular biosynthetic process organonitrogen compound biosynthetic process protein-containing complex disassembly regulation of protein-containing complex disassembly regulation of primary metabolic process cellular component organization post-transcriptional regulation of gene expression organic substance biosynthetic process translational termination cellular component organization or biogenesis regulation of biosynthetic process cellular component disassembly protein-containing complex organization cellular metabolic process regulation of protein metabolic process regulation of translational termination regulation of cellular metabolic process regulation of macromolecule metabolic process gene expression translation macromolecule biosynthetic process regulation of cellular biosynthetic process regulation of gene expression biosynthetic process regulation of translation regulation of macromolecule biosynthetic process regulation of metabolic process positive regulation of proteasomal protein catabolic process catabolic process positive regulation of protein metabolic process proteolysis involved in protein catabolic process positive regulation of biological process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process regulation of ubiquitin-dependent protein catabolic process positive regulation of metabolic process positive regulation of ubiquitin-dependent protein catabolic process regulation of proteolysis regulation of proteolysis involved in protein catabolic process modification-dependent macromolecule catabolic process proteolysis positive regulation of macromolecule metabolic process organonitrogen compound catabolic process proteasomal protein catabolic process protein catabolic process regulation of catabolic process positive regulation of protein catabolic process positive regulation of proteolysis involved in protein catabolic process positive regulation of catabolic process regulation of proteasomal ubiquitin-dependent protein catabolic process modification-dependent protein catabolic process positive regulation of proteolysis regulation of proteasomal protein catabolic process positive regulation of proteasomal ubiquitin-dependent protein catabolic process ubiquitin-dependent protein catabolic process organic substance catabolic process regulation of protein catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth X]	IPR006620	Prolyl 4-hydroxylase, alpha subunit	Domain
A [auth X]	IPR043044	TPA1/Ofd1, C-terminal	Homologous Superfamily
A [auth X]	IPR039558	Prolyl 3,4-dihydroxylase TPA1/OFD1, N-terminal domain	Domain
A [auth X]	IPR019601	Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain	Domain
A [auth X]	IPR005123	Oxoglutarate/iron-dependent dioxygenase	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.